Functions of the Hsp90 chaperone system: Lifting client proteins to new heights

International Journal of Biochemistry and Molecular Biology

Volumn 4, Issue 4, 2013, Pages 157-165

  Eckl, Julia M ^a   Richter, Klaus ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

ATPase cyle; Chaperone; Clients; Hsp90; Kinase; SHR

Indexed keywords

ADENOSINE TRIPHOSPHATE; CELL CYCLE PROTEIN 37; CHAPERONE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 INHIBITOR; NOVOBIOCIN; PROTEIN KINASE; RADICICOL; TANESPIMYCIN;

ALZHEIMER DISEASE; AMINO TERMINAL SEQUENCE; BINDING SITE; BREAST CANCER; CARBOXY TERMINAL SEQUENCE; CATALYSIS; DIMERIZATION; ENZYME INHIBITION; FRONTOTEMPORAL DEMENTIA; HUMAN; HYDROLYSIS; HYDROPHILICITY; MOLECULAR DYNAMICS; NONHUMAN; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN MOTIF; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; REVIEW; TAUOPATHY; VIRUS REPLICATION;

EID: 84890522100     PISSN: None     EISSN: 21524114     Source Type: Journal    
DOI: None     Document Type: Review

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